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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2005-1-21
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pubmed:abstractText |
Membrane recruitment of adaptor proteins is crucial for coupling antigen receptors to downstream signaling events. Despite the essential function of the B cell adaptor SLP-65, the mechanism of its recruitment to the plasma membrane is not yet understood. Here we show that a highly conserved leucine zipper in the SLP-65 N terminus is responsible for membrane association. Alterations in the N terminus abolished SLP-65 membrane localization and activity, both of which were restored by replacement of the N terminus with a myristoylation signal. The N terminus is an autonomous domain that confers specific localization and function when transferred to green fluorescent protein or the adaptor protein SLP-76. Our data elucidate the mechanism of SLP-65 membrane recruitment and suggest that leucine zipper motifs are essential interaction domains of signaling proteins.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1529-2908
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
204-10
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pubmed:dateRevised |
2007-11-8
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pubmed:meshHeading |
pubmed-meshheading:15654340-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:15654340-Amino Acid Sequence,
pubmed-meshheading:15654340-Animals,
pubmed-meshheading:15654340-Carrier Proteins,
pubmed-meshheading:15654340-Cell Line,
pubmed-meshheading:15654340-Cell Membrane,
pubmed-meshheading:15654340-Humans,
pubmed-meshheading:15654340-Leucine Zippers,
pubmed-meshheading:15654340-Mice,
pubmed-meshheading:15654340-Molecular Sequence Data,
pubmed-meshheading:15654340-Mutation,
pubmed-meshheading:15654340-Myristic Acid,
pubmed-meshheading:15654340-Phosphoproteins,
pubmed-meshheading:15654340-Protein Binding,
pubmed-meshheading:15654340-Protein Transport,
pubmed-meshheading:15654340-Receptors, Antigen, B-Cell,
pubmed-meshheading:15654340-Saccharomyces cerevisiae,
pubmed-meshheading:15654340-Sequence Alignment
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pubmed:year |
2005
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pubmed:articleTitle |
A leucine zipper in the N terminus confers membrane association to SLP-65.
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pubmed:affiliation |
Institute for Biology III, Albert-Ludwigs University of Freiburg and Max-Planck-Institute for Immunobiology, Stuebeweg 51, 79108 Freiburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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